Title : Identification of the glycosaminoglycan-attachment site of mouse invariant-chain proteoglycan core protein by site-directed mutagenesis
Abstract :
- The invariant chain (Ii) , a nonpolymorphic glycoprotein that associates with the immunoregulatory Ia proteins encoded by the major histocompatibility complex, has a proteoglycan form ( Ii-CS) that bears a chondroitin sulfate glycosaminoglycan
- In this proteoglycan form, Ii may remain associated with Ia at the cell surface
- Inhibitors that prevent the addition of glycosaminoglycan to Ii have been found to depress antigen-presenting function
- Ii does not have multiple candidate glycosaminoglycan-attachment sites, and we used site-directed mutagenesis to replace a candidate serine glycosaminoglycan-acceptor site with alanine at position 201 in the murine Ii protein
- Transfection of the normal or altered gene into Ii-negative COS-7 cells showed that equivalent amounts of core Ii protein and its acidic, terminally glycosylated forms were synthesized, but the Ala-201 mutant Ii did not give rise to Ii-CS
- The mutant protein had apparently normal transport through the Golgi compartment and associated stably with Ia molecules
- Thus, this mutation directly identifies the site of glycosaminoglycan addition and shows that it can be eliminated without adversely affecting the overall biosynthesis of Ii
Output (sent_index, trigger,
protein,
sugar,
site):
- 1. bears, , Ii, a chondroitin sulfate glycosaminoglycan, -
- 1. glycoprotein, , glycoprotein, -, -
- 1. has, , (Ii), a proteoglycan form, -
- 1. has, , glycoprotein, a proteoglycan form, -
- 4. have, , Ii, multiple candidate glycosaminoglycan-attachment sites, -
- 4. serine, , -, a candidate serine glycosaminoglycan-acceptor site, serine
Output(Part-Of) (sent_index,
protein,
site):
- 4. protein, alanine at position 201
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):